ID W9Z7M5_9EURO Unreviewed; 1026 AA.
AC W9Z7M5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831, ECO:0000256|RuleBase:RU367138};
DE EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
GN ORFNames=A1O1_03612 {ECO:0000313|EMBL:EXJ90509.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ90509.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ90509.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ90509.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the first alpha-1,4-linked mannose of the
CC glycosylphosphatidylinositol precursor of GPI-anchor.
CC {ECO:0000256|ARBA:ARBA00024850, ECO:0000256|RuleBase:RU367138}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU367138}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367138}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
CC {ECO:0000256|ARBA:ARBA00008400, ECO:0000256|RuleBase:RU367138}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ90509.1}.
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DR EMBL; AMWN01000003; EXJ90509.1; -; Genomic_DNA.
DR RefSeq; XP_007722703.1; XM_007724513.1.
DR AlphaFoldDB; W9Z7M5; -.
DR STRING; 1182541.W9Z7M5; -.
DR GeneID; 19158502; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR OrthoDB; 6598at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000019484; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16020; GPI_EPT_1; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007070; GPI_EtnP_transferase_1.
DR InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR PANTHER; PTHR12250:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 1; 1.
DR PANTHER; PTHR12250; PHOSPHATIDYLINOSITOL GLYCAN, CLASS N; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367138};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW ECO:0000256|RuleBase:RU367138};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367138};
KW Reference proteome {ECO:0000313|Proteomes:UP000019484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367138};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367138};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367138}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 459..484
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 496..515
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 521..539
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 560..579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 585..604
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 611..634
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 640..658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 678..696
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 716..733
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 740..758
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 838..859
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 879..899
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 911..930
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 936..959
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 449..935
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
SQ SEQUENCE 1026 AA; 113255 MW; D69B503E72E32E3A CRC64;
MARLGRGGFL GLAIVFHLVY VYSIFDIYFV SPIVHGMKPY KVEQDRAPSR RLVLFVGDGL
RADKAFQSFP DPSPADPANA DLILRPLAPF LRSRVLEHGT FGVSHTRVPT ESRPGHVALI
AGLYEDVSAV TTGWKLNPVD FDSVFNRSRH TWSWGSPDIL PMFKEGAVPG RVDADQYGEE
FEDFTQDATK LDTWVFDRVK ALFEAASSNS TLNAMLREDK LVFFLHLLGL DTTGHAYRPY
SKEYLHNIKV VDQGVEAITN LIDNFYADGK TSYVFTADHG MSDWGSHGDG HPDNTRTPLI
AWGAGVAQPD IYPDTIAPGH EDGFSADWGL DHIRRHDVDQ ADVAALMAYL AGLEFPVNSV
GKLPLSYLAA TVQEKASAAL VNVREVLEMY NVKEEQKKST SLRYQPYPPF SNVNGSVVDR
ISTIEAAIDS NHHEHAIELS LELFHHALQG LRYLQTYDWL FLRALITIGY LGWITFAVTT
VIDLHVLDGA VPDRRSLGST MTFASILVAL YSFFFIEKSP LTYYAYAFFP VFFWEEVFAR
RNALVSGFSV LFGHVKRPSD WILLLIQAIV FLGVIEALVQ SYFHRTIFTV CYVLGAFYPV
FHGADFVKKH LFLVLAWASG CLVLSTFTLL PVIKVEDADT ITAGGLLMFG AGLGYLLFEH
DITARSMSNS AQSQPNVVSR VLMGLQCGII LLTIIVTRSS VASLQAKQGL PLGNQVVGWF
VLVASLILPF VHRSAPNRHY LHRLVIIFLT FSPSFIILTI SYEGLFYVAF CSTLLAWVRL
EHAIQLHTVS HPTSAPSSSG SRLRPNGVTI TSTSAQSVTN LHPATTFRTL ALPDLRRALF
FLFFLQSAFF STGNIASISS FSLDAVYRLL PIFDPFSQGA LLLFKIMVPF AIISAALGIL
NRRLGLQSSA LFMTVMAVSD VMTLNFFWMV KDEGSWLDIG TTISHFVIGS LLCVFVAGLE
GVSHALISGV EVDDAFEDRV RSAGGVDVVE GTAKANGHGN GNNGMVKEVE AHDEVNRNVQ
EAAAGR
//
